4zms: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q8DNC2_STRR6 Q8DNC2_STRR6]  
[https://www.uniprot.org/uniprot/Q8DNC2_STRR6 Q8DNC2_STRR6]  
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== Publication Abstract from PubMed ==
Spr1814 of Streptococcus pneumoniae is a response regulator (RR) that belongs to the NarL/FixJ subfamily and has a four-helix helix-turn-helix DNA-binding domain. Here, the X-ray crystal structure of the full-length spr1814 in complex with a phosphate analogue beryllium fluoride (BeF3(-)) was determined at 2.0 A. This allows for a structural comparison with the previously reported full-length unphosphorylated spr1814. The phosphorylation of conserved aspartic acid residue of N-terminal receiver domain triggers a structural perturbation at the alpha4-beta5-alpha5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain.
Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region.,Park AK, Lee JH, Chi YM, Park H Biochem Biophys Res Commun. 2016 Apr 29;473(2):625-9. doi:, 10.1016/j.bbrc.2016.03.144. Epub 2016 Mar 30. PMID:27038544<ref>PMID:27038544</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==
*[[Response regulator 3D structure|Response regulator 3D structure]]
*[[Response regulator 3D structure|Response regulator 3D structure]]
== References ==
<references/>
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</StructureSection>
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Latest revision as of 12:03, 13 August 2026

Structure of the full-length response regulator spr1814 in complex with a phosphate analogue and B3C

4zms, resolution 1.90Å

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